Métadonnées
Afficher la notice complètePartager cette publication !
Structure of a heteropolymeric type 4 pilus from a monoderm bacterium
SHAHIN, Meriam
MRC Centre for Molecular Microbiology and Infection [Imperial College, London] [CMBI]
Voir plus >
MRC Centre for Molecular Microbiology and Infection [Imperial College, London] [CMBI]
SHAHIN, Meriam
MRC Centre for Molecular Microbiology and Infection [Imperial College, London] [CMBI]
MRC Centre for Molecular Microbiology and Infection [Imperial College, London] [CMBI]
VALETTE, Odile
Laboratoire de chimie bactérienne [LCB]
Institut de Microbiologie de la Méditerranée [IMM]
Laboratoire de chimie bactérienne [LCB]
Institut de Microbiologie de la Méditerranée [IMM]
PELICIC, Vladimir
Institut National de la Santé et de la Recherche Médicale [INSERM]
Laboratoire de chimie bactérienne [LCB]
Institut National de la Santé et de la Recherche Médicale [INSERM]
Laboratoire de chimie bactérienne [LCB]
FRONZES, Remi
Institut Européen de Chimie et Biologie [IECB]
Microbiologie Fondamentale et Pathogénicité [MFP]
< Réduire
Institut Européen de Chimie et Biologie [IECB]
Microbiologie Fondamentale et Pathogénicité [MFP]
Langue
EN
Article de revue
Ce document a été publié dans
Nature Communications. 2023-12, vol. 14, n° 1, p. 7143
Résumé en anglais
Abstract Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. ...Lire la suite >
Abstract Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. Recent advances in cryo-electron microscopy (cryo-EM) led to structures of several T4F, revealing that the long N-terminal α-helix (α1) – the trademark of pilins – packs in the centre of the filaments to form a hydrophobic core. In diderm bacteria – all available bacterial T4F structures are from diderm species – a portion of α1 is melted (unfolded). Here we report that this architecture is conserved in phylogenetically distant monoderm species by determining the structure of Streptococcus sanguinis T4P. Our 3.7 Å resolution cryo-EM structure of S. sanguinis heteropolymeric T4P and the resulting full atomic model including all minor pilins highlight universal features of bacterial T4F and have widespread implications in understanding T4F biology.< Réduire
Project ANR
Analyse structure/fonction du pilus Com, nanomachine filamenteuse répandue chez les bactéries monodermes, dédiée à la capture d'ADN - ANR-21-CE11-0008
Unités de recherche